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Q8VI36

- PAXI_MOUSE

UniProt

Q8VI36 - PAXI_MOUSE

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Protein

Paxillin

Gene

Pxn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).By similarity

GO - Molecular functioni

  1. BH4 domain binding Source: MGI
  2. receptor signaling complex scaffold activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of MAPK activity Source: MGI
  2. branching morphogenesis of an epithelial tube Source: MGI
  3. cellular component movement Source: MGI
  4. cytoskeleton organization Source: MGI
  5. focal adhesion assembly Source: MGI
  6. integrin-mediated signaling pathway Source: MGI
  7. lamellipodium assembly Source: MGI
  8. peptidyl-tyrosine phosphorylation Source: MGI
  9. positive regulation of protein kinase activity Source: MGI
  10. regulation of cell shape Source: MGI
  11. substrate adhesion-dependent cell spreading Source: MGI
  12. transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_206286. GAB1 signalosome.
REACT_235059. Smooth Muscle Contraction.
REACT_242946. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_255191. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_257088. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Paxillin
Gene namesi
Name:Pxn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:108295. Pxn.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcell cortex 1 Publication
Note: Colocalizes with integrins at the cell periphery.

GO - Cellular componenti

  1. cell leading edge Source: MGI
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. focal adhesion Source: MGI
  5. lamellipodium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591PaxillinPRO_0000075854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei31 – 311Phosphotyrosine; by PTK6By similarity
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei88 – 881Phosphotyrosine1 Publication
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei118 – 1181Phosphotyrosine; by PTK63 Publications
Modified residuei119 – 1191PhosphoserineBy similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei181 – 1811PhosphotyrosineBy similarity
Modified residuei244 – 2441Phosphoserine; by CDK5By similarity
Modified residuei322 – 3221PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by MAPK1/ERK2. Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation (By similarity). Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8VI36.
PaxDbiQ8VI36.
PRIDEiQ8VI36.

PTM databases

PhosphoSiteiQ8VI36.

Miscellaneous databases

PMAP-CutDBQ8VI36.

Expressioni

Gene expression databases

BgeeiQ8VI36.
CleanExiMM_PXN.
ExpressionAtlasiQ8VI36. baseline and differential.
GenevestigatoriQ8VI36.

Interactioni

Subunit structurei

Interacts with VCL and SRC (via SH3 domain). Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds ASAP2. Interacts with RNF5 and PDCD10 (By similarity). Interacts with SORBS1, PARVA and PARVB. Interacts with NEK3 and this interaction is prolactin-dependent (By similarity). Interacts with PTK2/FAK1. Interacts with PTK6 (By similarity). Interacts with PTK2B/PYK2. Interacts with CD36.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
L1camP116272EBI-983394,EBI-397964
Ptk2P341523EBI-983394,EBI-77070
PTPN1P180312EBI-983394,EBI-968788From a different organism.
VclQ647273EBI-983394,EBI-432047

Protein-protein interaction databases

BioGridi202525. 16 interactions.
IntActiQ8VI36. 20 interactions.
MINTiMINT-141924.

Structurei

3D structure databases

ProteinModelPortaliQ8VI36.
SMRiQ8VI36. Positions 357-590.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini356 – 41560LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini416 – 47358LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini474 – 53360LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST
Domaini534 – 59158LIM zinc-binding 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 1513LD motif 1Add
BLAST
Motifi144 – 15613LD motif 2Add
BLAST
Motifi216 – 22813LD motif 3Add
BLAST
Motifi265 – 27612LD motif 4Add
BLAST
Motifi333 – 34513LD motif 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi46 – 538Pro-rich

Sequence similaritiesi

Belongs to the paxillin family.Curated
Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG267887.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiQ8VI36.
KOiK05760.
OrthoDBiEOG70ZZQN.
PhylomeDBiQ8VI36.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
PRINTSiPR00832. PAXILLIN.
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Beta (identifier: Q8VI36-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP
60 70 80 90 100
PPPSSEALNG TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT
110 120 130 140 150
QDGVGSLCSR AGEEEHVYSF PNKQKSAEPS PTVMSSSLGS NLSELDRLLL
160 170 180 190 200
ELNAVQHSPP GFPADEAESS PPLPGALSPL YGIPENNTPL GGKAGPLVKE
210 220 230 240 250
KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS
260 270 280 290 300
SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR
310 320 330 340 350
QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV
360 370 380 390 400
ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD
410 420 430 440 450
GQPYCEKDYH SLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF
460 470 480 490 500
GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF
510 520 530 540 550
VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM
560 570 580 590
AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C
Length:591
Mass (Da):64,476
Last modified:March 1, 2002 - v1
Checksum:iB41A1892E6F60544
GO
Isoform Alpha (identifier: Q8VI36-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: Missing.

Show »
Length:557
Mass (Da):60,811
Checksum:i483D880CF16289B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711P → R in BAE42452. (PubMed:16141072)Curated
Sequence conflicti212 – 2121D → N in BAE34151. (PubMed:16141072)Curated
Sequence conflicti294 – 2941G → S in BAE34151. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 31134Missing in isoform Alpha. 2 PublicationsVSP_016357Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293883 mRNA. Translation: AAL71910.1.
AF293882 mRNA. Translation: AAL71909.1.
AK149933 mRNA. Translation: BAE29176.1.
AK157688 mRNA. Translation: BAE34151.1.
AK167299 mRNA. Translation: BAE39404.1.
AK171436 mRNA. Translation: BAE42452.1.
CCDSiCCDS19593.1. [Q8VI36-2]
CCDS39229.1. [Q8VI36-1]
RefSeqiNP_035353.1. NM_011223.3. [Q8VI36-2]
NP_598676.2. NM_133915.3.
UniGeneiMm.18714.

Genome annotation databases

EnsembliENSMUST00000067268; ENSMUSP00000069624; ENSMUSG00000029528. [Q8VI36-2]
GeneIDi19303.
KEGGimmu:19303.
UCSCiuc008zeb.1. mouse. [Q8VI36-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293883 mRNA. Translation: AAL71910.1 .
AF293882 mRNA. Translation: AAL71909.1 .
AK149933 mRNA. Translation: BAE29176.1 .
AK157688 mRNA. Translation: BAE34151.1 .
AK167299 mRNA. Translation: BAE39404.1 .
AK171436 mRNA. Translation: BAE42452.1 .
CCDSi CCDS19593.1. [Q8VI36-2 ]
CCDS39229.1. [Q8VI36-1 ]
RefSeqi NP_035353.1. NM_011223.3. [Q8VI36-2 ]
NP_598676.2. NM_133915.3.
UniGenei Mm.18714.

3D structure databases

ProteinModelPortali Q8VI36.
SMRi Q8VI36. Positions 357-590.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202525. 16 interactions.
IntActi Q8VI36. 20 interactions.
MINTi MINT-141924.

PTM databases

PhosphoSitei Q8VI36.

Proteomic databases

MaxQBi Q8VI36.
PaxDbi Q8VI36.
PRIDEi Q8VI36.

Protocols and materials databases

DNASUi 19303.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000067268 ; ENSMUSP00000069624 ; ENSMUSG00000029528 . [Q8VI36-2 ]
GeneIDi 19303.
KEGGi mmu:19303.
UCSCi uc008zeb.1. mouse. [Q8VI36-2 ]

Organism-specific databases

CTDi 5829.
MGIi MGI:108295. Pxn.

Phylogenomic databases

eggNOGi NOG267887.
GeneTreei ENSGT00760000118910.
HOGENOMi HOG000018764.
HOVERGENi HBG001512.
InParanoidi Q8VI36.
KOi K05760.
OrthoDBi EOG70ZZQN.
PhylomeDBi Q8VI36.

Enzyme and pathway databases

Reactomei REACT_206286. GAB1 signalosome.
REACT_235059. Smooth Muscle Contraction.
REACT_242946. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_255191. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_257088. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

ChiTaRSi Pxn. mouse.
NextBioi 296261.
PMAP-CutDB Q8VI36.
PROi Q8VI36.
SOURCEi Search...

Gene expression databases

Bgeei Q8VI36.
CleanExi MM_PXN.
ExpressionAtlasi Q8VI36. baseline and differential.
Genevestigatori Q8VI36.

Family and domain databases

Gene3Di 2.10.110.10. 4 hits.
InterProi IPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 4 hits.
[Graphical view ]
PRINTSi PR00832. PAXILLIN.
SMARTi SM00132. LIM. 4 hits.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytes."
    Chay K.O., Park S.S., Mushinski J.F.
    J. Biol. Chem. 277:14521-14529(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
    Strain: BALB/c.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
    Strain: C57BL/6J and NOD.
    Tissue: Placenta and Spleen.
  3. "The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells."
    Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A., Sattler M., Avraham H., Griffin J.D.
    J. Biol. Chem. 271:31222-31226(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2B/PYK2, SUBCELLULAR LOCATION.
  4. "Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells."
    Ku H., Meier K.E.
    J. Biol. Chem. 275:11333-11340(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPK1/ERK2.
  5. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
    Nikolopoulos S.N., Turner C.E.
    J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARVA.
  6. "The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin."
    Hayashi I., Vuori K., Liddington R.C.
    Nat. Struct. Biol. 9:101-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2/FAK1.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; TYR-88 AND TYR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Regulation of focal adhesions by flightless i involves inhibition of paxillin phosphorylation via a Rac1-dependent pathway."
    Kopecki Z., O'Neill G.M., Arkell R.M., Cowin A.J.
    J. Invest. Dermatol. 131:1450-1459(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-118.

Entry informationi

Entry nameiPAXI_MOUSE
AccessioniPrimary (citable) accession number: Q8VI36
Secondary accession number(s): Q3TB62, Q3TZQ6, Q8VI37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2002
Last modified: November 26, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3